Recombinant Rat Metalloproteinase Inhibitor 1 (TIMP1) Protein (His)

Name: Recombinant Rat Metalloproteinase Inhibitor 1 (TIMP1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-08247P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Rat Metalloproteinase Inhibitor 1 (TIMP1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P30120
Target Symbol	TIMP1
Synonyms	Timp1; Timp-1; Metalloproteinase inhibitor 1; Tissue inhibitor of metalloproteinases 1; TIMP-1
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	CSCAPTHPQTAFCNSDLVIRAKFMGSPEIIETTLYQRYEIKMTKMLKGFDAVGNATGFRFAYTPAMESLCGYVHKSQNRSEEFLIAGRLRNGNLHITACSFLVPWHNLSPAQQKAFVKTYSAGCGVCTVFPCSAIPCKLESDSHCLWTDQILMGSEKGYQSDHFACLPRNPDLCTWQYLGVSMTRSLPLAKAEA
Expression Range	24-217aa
Protein Length	Full Length of Mature Protein
Mol. Weight	25.5kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Also stimulates steroidogenesis by Leydig and ovarian granuloma cells; procathepsin L is required for maximal activity.
Subcellular Location	Secreted.
Protein Families	Protease inhibitor I35 (TIMP) family
Database References	KEGG: rno:116510 STRING: 10116.ENSRNOP00000013745 UniGene: PMID: 26252163 In a normoglycemic rat model of wound healing, pentoxifylline significantly increased TIMP-1 gene expression. PMID: 26087281 Our findings clearly demonstrate that despite their dramatic spatial rearrangement, cones and second-order neuron processes maintain their synaptic connections before and after TIMP-1 treatment. PMID: 26277580 Data indicate that adiponectin promoted tissue inhibitor of metalloproteinase-1 (TIMP-1) expression and limited hepatic stellate cell migration . PMID: 25575598 Basic fibroblast growth factor could up-regulate TIMP-1 expression and down-regulate MMP-9 activation in CFs in perivascular spaces, leading to inhibited progression of cardiac fibrosis during hypertensive heart failure. PMID: 24322055 Acute and chronic elevated laminar shear stress act to maintain vessel integrity through increasing TIMP-1 production, and the TGFbeta signaling pathway is essential to maintain TIMP-1 expression during chronic shear stress. PMID: 24471921 Inducible TIMP1 can modulate the expression of fibrosis-related genes in the liver. PMID: 23456624 Data indicate that increased TIMP-1 levels inhibit the proteolytic processing of Reelin under epileptic conditions. PMID: 23493620 study aimed to identify genomic biomarkers for early and sensitive detection of renal papillary injury in rats; Timp1, Igf1, and Lamc2 exhibited the best prediction performance PMID: 23142791 TIMP-1 increased in the rats treated with doxycycline ahead and might compensate for the activity of MMP-9 in lung injury following cardiopulmonary bypass. PMID: 22449799 Recombinant human TIMP-1 is distributed quickly into rat ischemic brain tissue and is slowly eliminated in both blood and brain tissue of rats. PMID: 21535944 Data show that the protein and mRNA expression level of TIMP-1 was high in asthmatic rat's lung tissues. PMID: 16191269 Dahuang Zhechong Pill can down-regulate the expressions of TIMP-1 and PAI-1 mRNAs in renal tissues of rats with focal segmental glomerulosclerosis. PMID: 18471418 higher levels of MMP-9 messenger RNA and protein expression were detected in the diabetic group compared with the control group (P < .05), and expression of TIMP-1 messenger RNA and protein was significantly decreased. PMID: 19917734 TIMPs are involved in cell viability and tissue remodelling in the ischemic brain PMID: 11860503 role of TIMP-1 in the airway extracellular matrix (ECM) remodelling of chronic obstructive pulmonary disease (COPD) rat models PMID: 12137602 TIMP-1 induction by ANG II in aortic smooth muscle cells occurs in the absence of histological changes at the vascular wall. PMID: 12388255 tissue inhibitor of metalloproteinase-1 mRNA was observed surrounding the developing corpus luteum (CL), with less intense expression present in granulosa-lutein cells PMID: 12444073 oxidative stress-stimulated up-regulation of TIMP-1 may play an important role in the deposition of collagen or extracellular matrix elements in the glomeruli during hyperhomocysteinemia. PMID: 12631082 TIMP-1 expression increased transiently but significantly during junction assembly in Sertoli cells and germ cells PMID: 12826691 An imbalance between collagenases and TIMPs, excessive gelatinolytic activity, and epithelial apoptosis participate in the fibrotic response in this experimental model. PMID: 12882763 TIMP1 gene transcription is regulated by RUNX1 and RUNX2 PMID: 15051730 Administration of anti-TIMP-1 resulted in a marked decrease in alpha-SMA staining. TIMP-1 antibody attenuated CCl(4)-induced liver fibrosis and decreased hepatic stellate cell activation and MMP-2 activity. PMID: 15389776 PANC-1 CM stimulates PSC proliferation and TIMP-1 through the MAP kinase (ERK 1/2) pathway. PMID: 15451430 TIMP-1 may play an important role in the process of liver aging PMID: 15968723 NO by induction of the Smad signaling pathway modulates TIMP-1 expression. PMID: 16183640 In immune-induced model of rat liver fibrosis, serum TIMP-1 level could reflect severity of liver fibrosis, while in CCL4-induced model, the correlation between the serum TIMP-1 level and the severity of hepatic fibrosis was not statistically significant PMID: 16718785 suggests a novel extracellular mechanism of late long-term potentiation in the PFC, engaging TIMP-1-controlled proteolysis as an element of information integration PMID: 17210139 Expression of Timp1 was decreased by treatment with the protective agent from Aspergillus. PMID: 17485851 Shear stress-induced Ets-1 modulates TIMP-1 expression in microvascular endothelial cells. PMID: 18636553 Gene expression of Timp1 fibroblasts from the medial collateral ligament, anterior cruciate ligament and patellar tendon was not significantly different. PMID: 18807189 W256 cells do not express or secrete TIMP-1 protein, although RT-PCR analysis indicated low-level TIMP-1 mRNA expression. PMID: 19330523 Increased expression of TIMP-1 in venous endothelium and plasma may serve as an early indicator of endothelial dysfunction. PMID: 19467832 These data are the first to show that the elevated vascular expression of TIMP-1, associated with breakdown of the blood-brain barrier following focal ischemia, are transcriptionally regulated via the MEK/ERK pathway. PMID: 19497125

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.